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5GGG

Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase form I

Functional Information from GO Data
ChainGOidnamespacecontents
A0006486biological_processprotein glycosylation
A0008375molecular_functionacetylglucosaminyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues161
DetailsDomain: {"description":"GG-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU01375","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues13
DetailsRegion: {"description":"Interaction with O-glycosylated substrate glycoprotein","evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5GGI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5GGI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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